3QTA
Crystal structure of a CheC-like protein (rrnAC0528) from Haloarcula marismortui ATCC 43049 at 2.00 A resolution
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL11-1 |
| Synchrotron site | SSRL |
| Beamline | BL11-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-01-27 |
| Detector | MARMOSAIC 325 mm CCD |
| Wavelength(s) | 0.91837,0.97958,0.97885 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 89.928, 89.928, 148.299 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.976 - 2.000 |
| R-factor | 0.1762 |
| Rwork | 0.175 |
| R-free | 0.20230 |
| Structure solution method | MAD |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.488 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.3.15) |
| Phasing software | SOLVE |
| Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 29.976 | 29.976 | 2.050 |
| High resolution limit [Å] | 2.000 | 8.940 | 2.000 |
| Rmerge | 0.011 | 0.011 | |
| Total number of observations | 3346 | 22338 | |
| Number of reflections | 41896 | ||
| <I/σ(I)> | 8.9 | 25.8 | 2 |
| Completeness [%] | 100.0 | 97.5 | 100 |
| Redundancy | 7.3 | 6 | 7.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 277 | 0.16M Ca(OAc)2, 20.0% Glycerol, 14.4% PEG-8000, 0.1M Cacodylate pH 6.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K |






